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Energy Transduction in Nitrogenase.

Lance C Seefeldt1,2, Brian M Hoffman3, John W Peters2,4

  • 1Department of Chemistry and Biochemistry , Utah State University , Logan , Utah 84322 , United States.

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|August 11, 2018
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Summary
This summary is machine-generated.

Nitrogenase enzyme uses ATP to convert nitrogen to ammonia. Electron transfer is gated by protein changes and ATP hydrolysis, with phosphate release being the rate-limiting step.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Bioenergetics

Background:

  • Nitrogenase is a complex enzyme catalyzing N2 reduction to NH3.
  • The Fe protein cycle is crucial for electron delivery to the MoFe protein.
  • Understanding nitrogenase mechanism is vital for nitrogen fixation research.

Purpose of the Study:

  • To elucidate the mechanism of electron transfer in the Fe protein cycle.
  • To investigate the role of ATP binding and hydrolysis in nitrogenase function.
  • To model the energy transduction process in nitrogenase.

Main Methods:

  • Osmotic pressure measurements to study electron transfer rates.
  • Analysis of protein conformational changes.
  • Kinetic studies of ATP hydrolysis and Pi release.

Main Results:

  • Electron transfer is gated by protein conformational changes.
  • ATP hydrolysis follows electron transfer and drives protein complex relaxation.
  • Phosphate release, not protein dissociation, is the rate-limiting step.
  • Anticooperative interactions exist between nitrogenase components.

Conclusions:

  • A working model for the nitrogenase machine is presented.
  • ATP energy is transduced to drive N2 reduction.
  • Anticooperative motion may regulate nitrogenase activity.